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ODPX_YEAST
ID   ODPX_YEAST              Reviewed;         410 AA.
AC   P16451; D6VUX5; E9P906;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 191.
DE   RecName: Full=Pyruvate dehydrogenase complex protein X component, mitochondrial;
DE   AltName: Full=Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex;
DE   AltName: Full=E3-binding protein;
DE   AltName: Full=Pyruvate dehydrogenase complex component E3BP;
DE   Flags: Precursor;
GN   Name=PDX1; OrderedLocusNames=YGR193C; ORFNames=G7579;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 31-60 AND
RP   192-206.
RX   PubMed=2682658; DOI=10.1073/pnas.86.22.8732;
RA   Behal R.H., Browning K.S., Hall T.B., Reed L.J.;
RT   "Cloning and nucleotide sequence of the gene for protein X from
RT   Saccharomyces cerevisiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:8732-8736(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7645350; DOI=10.1002/yea.320110609;
RA   Arroyo J., Garcia-Gonzalez M., Garcia-Saez M.I., Sanchez M., Nombela C.;
RT   "The complete sequence of a 9037 bp DNA fragment of the right arm of
RT   Saccharomyces cerevisiae chromosome VII.";
RL   Yeast 11:587-591(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [6]
RP   MUTAGENESIS.
RX   PubMed=2007123; DOI=10.1021/bi00225a015;
RA   Lawson J.E., Behal R.H., Reed L.J.;
RT   "Disruption and mutagenesis of the Saccharomyces cerevisiae PDX1 gene
RT   encoding the protein X component of the pyruvate dehydrogenase complex.";
RL   Biochemistry 30:2834-2839(1991).
RN   [7]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: Required for anchoring dihydrolipoamide dehydrogenase (E3) to
CC       the dihydrolipoamide transacetylase (E2) core of the pyruvate
CC       dehydrogenase complexes of eukaryotes. This specific binding is
CC       essential for a functional PDH complex.
CC   -!- SUBUNIT: Eukaryotic pyruvate dehydrogenase (PDH) complexes are
CC       organized as a core consisting of the oligomeric dihydrolipoamide
CC       acetyl-transferase (E2), around which are arranged multiple copies of
CC       pyruvate dehydrogenase (E1), dihydrolipoamide dehydrogenase (E3) and
CC       protein X (E3BP) bound by non-covalent bonds.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- MISCELLANEOUS: Present with 414 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; M28222; AAA34910.1; -; Genomic_DNA.
DR   EMBL; X82408; CAA57804.1; -; Genomic_DNA.
DR   EMBL; Z72978; CAA97219.1; -; Genomic_DNA.
DR   EMBL; AY692983; AAT93002.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08286.1; -; Genomic_DNA.
DR   PIR; A36183; DEBYPX.
DR   RefSeq; NP_011709.1; NM_001181322.1.
DR   AlphaFoldDB; P16451; -.
DR   SMR; P16451; -.
DR   BioGRID; 33446; 77.
DR   ComplexPortal; CPX-3207; Mitochondrial pyruvate dehydrogenase complex.
DR   DIP; DIP-5550N; -.
DR   IntAct; P16451; 10.
DR   MINT; P16451; -.
DR   STRING; 4932.YGR193C; -.
DR   SwissPalm; P16451; -.
DR   MaxQB; P16451; -.
DR   PaxDb; P16451; -.
DR   PRIDE; P16451; -.
DR   EnsemblFungi; YGR193C_mRNA; YGR193C; YGR193C.
DR   GeneID; 853107; -.
DR   KEGG; sce:YGR193C; -.
DR   SGD; S000003425; PDX1.
DR   VEuPathDB; FungiDB:YGR193C; -.
DR   eggNOG; KOG0557; Eukaryota.
DR   HOGENOM; CLU_035825_2_1_1; -.
DR   InParanoid; P16451; -.
DR   OMA; VTKNRFE; -.
DR   BioCyc; YEAST:YGR193C-MON; -.
DR   PRO; PR:P16451; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P16451; protein.
DR   GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; IDA:ComplexPortal.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0005198; F:structural molecule activity; IDA:SGD.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IDA:SGD.
DR   Gene3D; 4.10.320.10; -; 1.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR045257; E2/Pdx1.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR23151; PTHR23151; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Lipoyl; Mitochondrion; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..30
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:2682658"
FT   CHAIN           31..410
FT                   /note="Pyruvate dehydrogenase complex protein X component,
FT                   mitochondrial"
FT                   /id="PRO_0000020487"
FT   DOMAIN          32..108
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   DOMAIN          169..210
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT   MOD_RES         73
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT                   ProRule:PRU01066"
FT   CONFLICT        378
FT                   /note="I -> M (in Ref. 5; AAT93002)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   410 AA;  45362 MW;  11649CA28C420CDF CRC64;
     MLSAISKVST LKSCTRYLTK CNYHASAKLL AVKTFSMPAM SPTMEKGGIV SWKYKVGEPF
     SAGDVILEVE TDKSQIDVEA LDDGKLAKIL KDEGSKDVDV GEPIAYIADV DDDLATIKLP
     QEANTANAKS IEIKKPSADS TEATQQHLKK ATVTPIKTVD GSQANLEQTL LPSVSLLLAE
     NNISKQKALK EIAPSGSNGR LLKGDVLAYL GKIPQDSVNK VTEFIKKNER LDLSNIKPIQ
     LKPKIAEQAQ TKAADKPKIT PVEFEEQLVF HAPASIPFDK LSESLNSFMK EAYQFSHGTP
     LMDTNSKYFD PIFEDLVTLS PREPRFKFSY DLMQIPKANN MQDTYGQEDI FDLLTGSDAT
     ASSVRPVEKN LPEKNEYILA LNVSVNNKKF NDAEAKAKRF LDYVRELESF
 
 
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